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Modification of simian virus 40 large tumor antigen by glycosylation

The SV40-encoded transforming protein, large tumor antigen (T-ag), is multifunctional. Chemical modifications of the T-ag polypeptide may be important for its multifunctional capacity. T-ag is additionally modified by glycosylation. T-ag was metabolically labeled in SV40-infected cells with tritiate...

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Autores principales: Jarvis, Donald L., Butel, Janet S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Inc. 1985
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130735/
https://www.ncbi.nlm.nih.gov/pubmed/3002015
http://dx.doi.org/10.1016/0042-6822(85)90250-8
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author Jarvis, Donald L.
Butel, Janet S.
author_facet Jarvis, Donald L.
Butel, Janet S.
author_sort Jarvis, Donald L.
collection PubMed
description The SV40-encoded transforming protein, large tumor antigen (T-ag), is multifunctional. Chemical modifications of the T-ag polypeptide may be important for its multifunctional capacity. T-ag is additionally modified by glycosylation. T-ag was metabolically labeled in SV40-infected cells with tritiated galactose or glucosamine, but not with mannose or fucose. The identity of glycosylated T-ag was established by immunoprecipitation with a variety of T-ag-specific antisera, including monoclonal antibodies. Incorporation of labeled sugar into T-ag was inhibited in the presence of excess unlabeled sugars, but not in the presence of excess unlabeled amino acids. Labeled monosaccharides could be preferentially removed from T-ag with a mixture of glycosidic enzymes. In addition, galactose was removed from purified T-ag by acid hydrolysis and identified as such by thin-layer chromatography. T-ag oligosaccharides were resistant to treatment with EndoH, and glycosylation was not inhibited by tunicamycin. Together, these data strongly suggest that T-ag is glycosylated. Several characteristics, including lack of mannose labeling, EndoH resistance, and tunicamycin resistance, suggest that T-ag is not an N-linked glycoprotein. Rather, these properties are more consistent with the identification of T-ag as an O-linked glycoprotein.
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spelling pubmed-71307352020-04-08 Modification of simian virus 40 large tumor antigen by glycosylation Jarvis, Donald L. Butel, Janet S. Virology Article The SV40-encoded transforming protein, large tumor antigen (T-ag), is multifunctional. Chemical modifications of the T-ag polypeptide may be important for its multifunctional capacity. T-ag is additionally modified by glycosylation. T-ag was metabolically labeled in SV40-infected cells with tritiated galactose or glucosamine, but not with mannose or fucose. The identity of glycosylated T-ag was established by immunoprecipitation with a variety of T-ag-specific antisera, including monoclonal antibodies. Incorporation of labeled sugar into T-ag was inhibited in the presence of excess unlabeled sugars, but not in the presence of excess unlabeled amino acids. Labeled monosaccharides could be preferentially removed from T-ag with a mixture of glycosidic enzymes. In addition, galactose was removed from purified T-ag by acid hydrolysis and identified as such by thin-layer chromatography. T-ag oligosaccharides were resistant to treatment with EndoH, and glycosylation was not inhibited by tunicamycin. Together, these data strongly suggest that T-ag is glycosylated. Several characteristics, including lack of mannose labeling, EndoH resistance, and tunicamycin resistance, suggest that T-ag is not an N-linked glycoprotein. Rather, these properties are more consistent with the identification of T-ag as an O-linked glycoprotein. Published by Elsevier Inc. 1985-03 2004-02-06 /pmc/articles/PMC7130735/ /pubmed/3002015 http://dx.doi.org/10.1016/0042-6822(85)90250-8 Text en Copyright © 1985 Published by Elsevier Inc. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Jarvis, Donald L.
Butel, Janet S.
Modification of simian virus 40 large tumor antigen by glycosylation
title Modification of simian virus 40 large tumor antigen by glycosylation
title_full Modification of simian virus 40 large tumor antigen by glycosylation
title_fullStr Modification of simian virus 40 large tumor antigen by glycosylation
title_full_unstemmed Modification of simian virus 40 large tumor antigen by glycosylation
title_short Modification of simian virus 40 large tumor antigen by glycosylation
title_sort modification of simian virus 40 large tumor antigen by glycosylation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130735/
https://www.ncbi.nlm.nih.gov/pubmed/3002015
http://dx.doi.org/10.1016/0042-6822(85)90250-8
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